• Gamma-synuclein is a protein that in humans is encoded by the SNCG gene. (wikipedia.org)
  • Gamma-synuclein is a synuclein protein found primarily in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. (wikipedia.org)
  • Gamma-synuclein is the least conserved of the synuclein proteins. (wikipedia.org)
  • Gamma-Synucleins expression in breast tumors is a marker for tumor progression as mammalian gamma-synuclein was first identified as breast cancer-specific gene 1 (BCSG1). (wikipedia.org)
  • A change in the expression of gamma-synuclein has been observed in the retina of patients with Alzheimer's disease. (wikipedia.org)
  • The normal cellular function of gamma-synuclein remains unknown. (wikipedia.org)
  • Gamma-synuclein has been shown to interact with BUB1B. (wikipedia.org)
  • Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. (affbiotech.cn)
  • Parkinson's disease (PD) is a neurodegenerative disorder characterized by death of dopaminergic neurons in the substantia nigra (SN) and accumulation of α-Synuclein in intracellular inclusions known as Lewy bodies (LBs) [ 1 - 10 ]. (biomedcentral.com)
  • Phospho-Synuclein alpha (Tyr133) Antibody detects endogenous levels of Synuclein alpha only when phosphorylated at Tyrosine 133. (affbiotech.cn)
  • Alpha-synuclein (SNCA) as the presynaptic protein is expressed in different tissues and prevents insulin-resistance (IR) through increasing glucose-uptake by adipocytes and muscles. (biomedcentral.com)
  • Alpha-synuclein (SNCA, α-Syn) as one of the members of synuclein protein family is mainly expressed in brain tissue. (biomedcentral.com)
  • We tested how these two genes interact by examining the effects of parkin on post-translational modification of α-Synuclein in gene transfer animal models, using a lentiviral gene delivery system into the striatum of 2-month old male Sprague Dawley rats. (biomedcentral.com)
  • α-Synuclein aggregates in Lewy bodies and plays a central role in the pathogenesis of a group of neurodegenerative disorders, known as "Synucleinopathies", including Parkinson's disease. (biomedcentral.com)
  • Viral expression of wild type α-Synuclein caused accumulation of α-Synuclein and was associated with increased cell death and inflammation. (biomedcentral.com)
  • It has reported that decreased levels of plasma alpha-synuclein were associated with insulin resistance. (biomedcentral.com)
  • α-Synuclein increased PLK2 levels and GSK-3β activity and increased the levels of phosphorylated α-Synuclein and Tau. (biomedcentral.com)
  • Parkin co-expression reduced the levels of phosphorylated α-Synuclein and attenuated cell death and inflammation. (biomedcentral.com)
  • These data suggest that parkin reduces α-Synuclein levels and alters the balance between phosphatase and kinase activities that affect the levels of phosphorylated α-Synuclein. (biomedcentral.com)
  • Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. (affbiotech.cn)
  • Mutations in and alterations in expression levels of alpha-synuclein cause autosomal dominant early onset heredity forms of Parkinson's disease, and sporadic Parkinson's disease is defined in part by the presence of Lewy bodies and Lewy neurites that are composed primarily of alpha-synuclein deposited in an aggregated amyloid fibril state. (en-journal.org)
  • Despite the difference in core elements of deposits in each neurodegenerative disorder, the cascade of neuronal reactions such as activation of glycogen synthase kinase-3 beta, mitogen-activated protein kinases, cell cycle re-entry and oxidative stress leading to a progressive neurodegeneration are surprisingly similar. (sagepub.com)
  • Synuclein-gamma is a member of the synuclein family of proteins, which are believed to be involved in the pathogenesis of neurodegenerative diseases. (wikipedia.org)
  • This review focuses on protein toxicity in two neurodegenerative diseases, AD and PD. (sagepub.com)
  • Keywords: Alzheimer's disease, Parkinson's disease, Beta-amyloid, Alpha-synuclein, Intracellular signalling, Neurotoxicity, Neurodegeneration Pathophysiology of toxic proteins Background All the proteins implicated in neurodegenerative diseases Protein misfolding and aggregation contribute to the share the common pattern of dysfunctional structure pathophysiology of neurodegenerative disorders such as due to an unusual folding [5-7]. (sagepub.com)
  • Neuronal response in Alzheimer's and Parkinson's disease: the effect of toxic proteins on. (sagepub.com)
  • Alpha-synuclein is a small neuronal protein that is closely associated with the etiology of Parkinson's disease. (en-journal.org)
  • We reviewed the activated mechanisms of neurotoxicity in response to misfolded beta-amyloid and α-synuclein, two major toxic proteins in AD and PD, leading to neuronal apoptosis. (sagepub.com)
  • The plaques was obtained for both Aβ 1-40 and 1-42, two of the most are the consequences of abnormal protein folding and toxic forms of amyloid protein [35, 36]. (sagepub.com)
  • Extra- Aβ, the principle protein implicated in development of cellular Aβ is internalized, stored in the lysosomes and AD, is derived from amyloid precursor protein (APP). (sagepub.com)
  • Several studies suggest a synergistic relationship between amyloid-β (Aβ) and α-synuclein (α-syn) accumulation. (biomedcentral.com)
  • folded proteins, may result in damage and progression of When an aggregation status is established, disaggregation neurodegenerative disorders [1, 2]. (sagepub.com)
  • Unfortunately, not all rarely occurs because under physiological conditions, the cellular responses to misfolded proteins are neuro- the equilibrium is in favour of aggregation [8-11]. (sagepub.com)
  • These interactions are considered critical for at least some normal functions of alpha-synuclein, and may well play critical roles in both the aggregation of the protein and its mechanisms of toxicity. (en-journal.org)
  • Alpha synuclein's contribution to such disorders could in principle result either from a toxic gain of function resulting from synuclein oligomerization and/or aggregation, or from a loss or perturbation of normal synuclein function (or possibly from a combination of the two). (en-journal.org)
  • Grantham, Hugh 2015-10-23 00:00:00 Accumulation of protein aggregates is the leading cause of cellular dysfunction in neurodegenerative disorders. (sagepub.com)
  • can leak into the cytosol by destabilization of the lyso- More than ten isoforms of the protein are characterized some membrane. (sagepub.com)
  • Here we review the known features of alpha-synuclein membrane interactions in the context of both the putative functions of the protein and of its pathological roles in disease. (en-journal.org)
  • We have explored the relationship between Aβ accumulation and the phosphorylation of α-syn at serine-129 (pSer129 α-syn), in post-mortem human brain tissue and in SH-SY5Y neuroblastoma cells transfected to overexpress human α-syn. (biomedcentral.com)
  • The interaction between the proteins in producing an overlapping pathological pattern will be also discussed. (sagepub.com)
  • Gamma-synuclein is a synuclein protein found primarily in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. (wikipedia.org)
  • Although alpha-synuclein is a highly soluble, cytoplasmic protein, it binds to a variety of cellular membranes of different properties and compositions. (en-journal.org)
  • Arp2-3 complex binds WASP PROTEIN and existing ACTIN FILAMENTS, and it nucleates the formation of new branch point filaments. (nih.gov)
  • HN - 2006 BX - Arp2-3 Complex MH - Actin-Related Protein 3 UI - D051378 MN - D5.750.78.730.246.750 MN - D12.776.220.525.246.750 MS - A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. (nih.gov)
  • Extracellular Aβ toxicity could be mediated through binding to receptors such as NMDA and dis- Aβ biochemical structure and toxicity rupting the calcium balance of the neuron [37, 38]. (sagepub.com)
  • The normal function of alpha-synuclein is poorly understood, and the precise mechanisms by which it leads to toxicity and cell death are also unclear. (en-journal.org)
  • Gamma-Synucleins expression in breast tumors is a marker for tumor progression as mammalian gamma-synuclein was first identified as breast cancer-specific gene 1 (BCSG1). (wikipedia.org)
  • HN - 2006(1998) MH - Actin-Related Protein 2-3 Complex UI - D051376 MN - D5.750.78.730.246 MN - D12.776.220.525.246 MS - A complex of seven proteins including ARP2 PROTEIN and ARP3 PROTEIN that plays an essential role in maintenance and assembly of the CYTOSKELETON. (nih.gov)
  • Similar repeat sequences are found in the exchangeable apolipoproteins, and as for many apolipoproteins, the N-terminal lipid-binding domain of alpha synuclein adopts an amphipathic helical structure upon binding to detergent micelles or phospholipid vesicles. (en-journal.org)
  • HN - 2006(1981) BX - Actin-Capping Proteins MH - Actin Depolymerizing Factors UI - D051339 MN - D5.750.78.730.212 MN - D12.776.220.525.212 MS - A family of low MOLECULAR WEIGHT actin-binding proteins found throughout eukaryotes. (nih.gov)
  • The N-terminal ~100 residues of the protein constitute a lipid-binding domain that contains 7 imperfect 11-residue repeats, each centered on a variation of a KTKEGV core consensus sequence. (en-journal.org)
  • HN - 2006(1981) BX - Cofilins MH - Actin-Related Protein 2 UI - D051377 MN - D5.750.78.730.246.500 MN - D12.776.220.525.246.500 MS - A PROFILIN binding domain protein that is part of the Arp2-3 complex. (nih.gov)
  • Any delay detecting the mis- functional structure, building a toxic protein deposition. (sagepub.com)